BMRB Entry 15940

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15940

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Title:
Association of subunit d (Vma6p) and E (Vma4p) with G (Vma10p) and the NMR solution structure of subunit G (G1-59) of the Saccharomyces cerevisiae V1VO ATPase
Deposition date:
2008-09-04
Original release date:
2009-03-20
Authors:
Sankaranarayanan, Rishikesan; Gayen, Shovanlal; Thaker, Youg raj; Subramanian, Vivekanandan; Manimekalai, Malathy; Gruber, Gerhard
Citation:

Citation: Rishikesan, Sankaranarayanan; Gayen, Shovanlal; Thaker, Youg raj; Vivekanandan, Subramanian; Manimekalai, Malathy; Yau, Yin; Shochata, Susana; Gruber, Gerhard. "Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G(1-59)) of the Saccharomyces cerevisiae V(1)V(O) ATPase"  Biochim. Biophys Acta. 1787, 242-251 (2009).
PubMed: 19344662

Assembly members:

Assembly members:
subunit G, polymer, 60 residues, 6969.088 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
subunit G: MVSQKNGIATLLQAEKEAHE IVSKARKYRQDKLKQAKTDA AKEIDSYKIQKDKELKEFEC

Data sets:
Data typeCount
13C chemical shifts237
15N chemical shifts55
1H chemical shifts390

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit G1

Entities:

Entity 1, subunit G 60 residues - 6969.088 Da.

1   METVALSERGLNLYSASNGLYILEALATHR
2   LEULEUGLNALAGLULYSGLUALAHISGLU
3   ILEVALSERLYSALAARGLYSTYRARGGLN
4   ASPLYSLEULYSGLNALALYSTHRASPALA
5   ALALYSGLUILEASPSERTYRLYSILEGLN
6   LYSASPLYSGLULEULYSGLUPHEGLUCYS

Samples:

sample_1: entity, [U-13C; U-15N], 1 mM; sodium phosphate 25 ± 0.3 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, P.GUNTERT ET AL. - structure calculation

TOPSPIN, Bruker Biospin - data acuisition and processing

SPARKY, Goddard - chemical shift assignment

Molmol, Koradi, Billeter and Wuthrich - viewing the final structure

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA23755
EMBL CAY80326
GB AAA74570 AAB68921 AHY77737 AJP39136 AJU16333
REF NP_011905
SP P48836
TPG DAA06731
AlphaFold P48836

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks